P0ABR9 (MHPB_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 61.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase EC=1.13.11.16 Alternative name(s): 3-carboxyethylcatechol 2,3-dioxygenase | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 314 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively. Ref.6 |
| Catalytic activity | 3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate. HAMAP-Rule MF_01653 (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate. HAMAP-Rule MF_01653 |
| Pathway | Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule MF_01653 |
| Subunit structure | Homotetramer. Ref.6 |
| Sequence similarities | Belongs to the LigB/MhpB extradiol dioxygenase family. |
| Biophysicochemical properties | Kinetic parameters: KM=26 µM for 2,3-dihydroxyphenylpropionic acid (at 20 degrees Celsius and pH 8) Ref.1 Ref.6 KM=36 µM for 2,3-dihydroxycinnamic acid (at 20 degrees Celsius and pH 8) KM=37 µM for methyl-2,3-dihydroxyphenylpropionate (at 20 degrees Celsius and pH 8) KM=90 µM for 3-methylcatechol (at 20 degrees Celsius and pH 8) KM=94 µM for 3-phenethylcatechol (at 20 degrees Celsius and pH 8) KM=154 µM for 3-propylcatechol (at 20 degrees Celsius and pH 8) KM=185 µM for 3-ethylcatechol (at 20 degrees Celsius and pH 8) KM=300 µM for 2,3-dihydroxyphenoxyacetic acid (at 20 degrees Celsius and pH 8) KM=700 µM for catechol (at 20 degrees Celsius and pH 8) |
Ontologies
| Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | Iron |
| Molecular function | Dioxygenase Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | 3-(3-hydroxy)phenylpropionate catabolic process Inferred from mutant phenotype PubMed 3531186. Source: EcoCyc 3-phenylpropionate catabolic processInferred from electronic annotation. Source: UniProtKB-UniPathway phenylpropanoid catabolic processInferred from mutant phenotype PubMed 3531186. Source: EcoCyc |
| Molecular_function | 3-carboxyethylcatechol 2,3-dioxygenase activity Inferred from direct assay Ref.6. Source: EcoCyc ferrous iron bindingInferred from direct assay Ref.6. Source: EcoCyc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 314 | 314 | 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase HAMAP-Rule MF_01653 | PRO_0000085103 | |||||
Sites | |||||||||
| Active site | 115 | 1 | Proton donor | ||||||
| Active site | 179 | 1 | Proton acceptor | ||||||
Experimental info | |||||||||
| Mutagenesis | 114 | 1 | D → A: Complete loss of extradiol cleavage activity. Ref.7 | ||||||
| Mutagenesis | 114 | 1 | D → N: Low level of catalytic activity, 600-fold lower than the wild-type enzyme. More than 8000-fold decrease in affinity. Ref.7 | ||||||
| Mutagenesis | 115 | 1 | H → A: Complete loss of extradiol cleavage activity. Ref.7 | ||||||
| Mutagenesis | 115 | 1 | H → Q: Complete loss of activity. Ref.7 | ||||||
| Mutagenesis | 115 | 1 | H → Y: Complete loss of activity. Ref.7 | ||||||
| Mutagenesis | 179 | 1 | H → A: Complete loss of activity. Ref.7 | ||||||
| Mutagenesis | 179 | 1 | H → Q: Complete loss of activity. Ref.7 | ||||||
| Mutagenesis | 179 | 1 | H → Y: Complete loss of activity. Ref.7 | ||||||
| Mutagenesis | 181 | 1 | P → A: More than 2-fold decrease in catalytic activity and 100-fold decrease in affinity. Ref.7 | ||||||
| Mutagenesis | 181 | 1 | P → H: More than 60-fold decrease in catalytic activity and affinity. Ref.7 | ||||||
| Sequence conflict | 138 – 140 | 3 | ING → NKA in BAA13053. Ref.1 | ||||||
| Sequence conflict | 152 | 1 | R → H in BAA13053. Ref.1 | ||||||
| Sequence conflict | 157 | 1 | A → T in BAA13053. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases." Spence E.L., Kawamukai M., Sanvoisin J., Braven H., Bugg T.D.H. J. Bacteriol. 178:5249-5256(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], BIOPHYSICOCHEMICAL PROPERTIES. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [2] | "Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12." Ferrandez A., Garcia J.L., Diaz E. J. Bacteriol. 179:2573-2581(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / CS520. |
| [3] | "Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [5] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [6] | "Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli." Bugg T.D.H. Biochim. Biophys. Acta 1202:258-264(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15, SUBUNIT, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. |
| [7] | "Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB)." Mendel S., Arndt A., Bugg T.D.H. Biochemistry 43:13390-13396(2004) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASP-114; HIS-115; HIS-179 AND PRO-181, REACTION MECHANISM. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D86239 Genomic DNA. Translation: BAA13053.1. Y09555 Genomic DNA. Translation: CAA70748.1. U73857 Genomic DNA. Translation: AAB18072.1. U00096 Genomic DNA. Translation: AAC73451.1. AP009048 Genomic DNA. Translation: BAE76130.1. |
| PIR | D64762. |
| RefSeq | NP_414882.1. NC_000913.2. YP_488642.1. NC_007779.1. |
3D structure databases | |
| ProteinModelPortal | P0ABR9. |
| SMR | P0ABR9. Positions 43-204. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P0ABR9. 5 interactions. |
| STRING | 511145.b0348. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAC73451; AAC73451; b0348. BAE76130; BAE76130; BAE76130. |
| GeneID | 12931736. 945047. |
| KEGG | ecj:Y75_p0337. eco:b0348. |
| PATRIC | 32115829. VBIEscCol129921_0356. |
Organism-specific databases | |
| EchoBASE | EB4167. |
| EcoGene | EG20274. mhpB. |
Phylogenomic databases | |
| eggNOG | NOG08474. |
| HOGENOM | HOG000069851. |
| KO | K05713. |
| OMA | AHEIRTW. |
| ProtClustDB | PRK13370. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:DHPDIOXYGEN-MONOMER. ECOL316407:JW0339-MONOMER. MetaCyc:DHPDIOXYGEN-MONOMER. |
| BRENDA | 1.13.11.16. 2026. |
| SABIO-RK | P0ABR9. |
| UniPathway | UPA00714. |
Gene expression databases | |
| Genevestigator | P0ABR9. |
Family and domain databases | |
| Gene3D | 3.40.830.10. 2 hits. |
| HAMAP | MF_01653. MhpB. |
| InterPro | IPR023789. DHPP/DHXA_dioxygenase. IPR004183. Xdiol_dOase_suB. [Graphical view] |
| Pfam | PF02900. LigB. 1 hit. [Graphical view] |
| SUPFAM | SSF53213. Xdiol_dOase_3B. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MHPB_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0ABR9 Secondary accession number(s): P54711 Q2MC76 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
